DRDI_CLOBH
ID DRDI_CLOBH Reviewed; 349 AA.
AC A5I1A6; A7G307;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=5-deoxyribose 1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_02229};
DE EC=5.3.1.- {ECO:0000255|HAMAP-Rule:MF_02229};
GN Name=drdI {ECO:0000255|HAMAP-Rule:MF_02229};
GN OrderedLocusNames=CBO1268, CLC_1306;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- FUNCTION: Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1-
CC phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose
CC salvage pathway that recycles this toxic radical SAM enzyme by-product
CC to mainstream metabolites. {ECO:0000255|HAMAP-Rule:MF_02229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-deoxy-alpha-D-ribose 1-phosphate = 5-deoxy-D-ribulose 1-
CC phosphate; Xref=Rhea:RHEA:61296, ChEBI:CHEBI:58749,
CC ChEBI:CHEBI:144504; Evidence={ECO:0000255|HAMAP-Rule:MF_02229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61297;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02229};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02229}.
CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC DrdI subfamily. {ECO:0000255|HAMAP-Rule:MF_02229}.
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DR EMBL; CP000727; ABS37413.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL82818.1; -; Genomic_DNA.
DR RefSeq; WP_011948892.1; NC_009698.1.
DR RefSeq; YP_001253792.1; NC_009495.1.
DR RefSeq; YP_001387172.1; NC_009698.1.
DR AlphaFoldDB; A5I1A6; -.
DR SMR; A5I1A6; -.
DR GeneID; 5185523; -.
DR KEGG; cbh:CLC_1306; -.
DR KEGG; cbo:CBO1268; -.
DR PATRIC; fig|413999.7.peg.1254; -.
DR HOGENOM; CLU_016218_1_2_9; -.
DR OMA; RLWVDET; -.
DR PRO; PR:A5I1A6; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR HAMAP; MF_02229; Deoxyribose1P_isomerase; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR043679; Deoxyribose1P_isomerase_DrdI.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR005251; IF-M1Pi.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..349
FT /note="5-deoxyribose 1-phosphate isomerase"
FT /id="PRO_0000357163"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT BINDING 49..51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT BINDING 250..251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT SITE 160
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
SQ SEQUENCE 349 AA; 38726 MW; 8310EDBBCF138B97 CRC64;
MAELLAIKWD DNRDKLILLD QTILPNKIEY IEYDTAEGVY DSIKDMIVRG APAIGVTAAY
GLYFAAKVAP EDKFENFFKY LKEKSSYLDS SRPTAVNLSW ALKVMESKAL ENKDKDVKEI
KSILREEAKR IHEEDIEICK TIGENLITLL KDGVGILTHC NAGQLATSKY GTATSPMYLA
KEKGWNFKVY SDETRPRLQG STLTALELYE AGIDVTTITD NMAAMVMSQG KIDAVIVGCD
RIAANGDTAN KIGTMGVSIL AKYFGIPMYI AAPTPSIDIN TKTGEDIPIE ERNPEEVTSR
FGVWTAPKGV KVYNPGFDVT PHENITAIVT EKGIVYPPFK ENLKKLFEK
